1CQU

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9

Summary for 1CQU

• Entry DOI: 10.2210/pdb1cqu/pdb
• NMR Information: BMRB: 4551
• Descriptor: 50S RIBOSOMAL PROTEIN L9 (1 entity in total)
• Functional Keywords: protein l9, ribosome
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 6231.31

Authors

Hua, Y.,Kuhlman, B.,Hoffman, D.,Raleigh, D.P. (deposition date: 1999-08-11, release date: 2002-04-27, Last modification date: 2024-05-22)

Primary citation

Luisi, D.L.,Kuhlman, B.,Sideras, K.,Evans, P.A.,Raleigh, D.P.
Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.
J.Mol.Biol., 289:167-174, 1999

PubMed Abstract: The N-terminal domain of the ribosomal protein L9 forms a split betaalphabeta structure with a long C-terminal helix. The folding transitions of a 56 residue version of this protein have previously been characterized, here we report the results of a study of a truncation mutant corresponding to residues 1-51. The 51 residue protein adopts the same fold as the 56 residue protein as judged by CD and two-dimensional NMR, but it is less stable as judged by chemical and thermal denaturation experiments. Studies with synthetic peptides demonstrate that the C-terminal helix of the 51 residue version has very little propensity to fold in isolation in contrast to the C-terminal helix of the 56 residue variant. The folding rates of the two proteins, as measured by stopped-flow fluorescence, are essentially identical, indicating that formation of local structure in the C-terminal helix is not involved in the rate-limiting step of folding.

PubMed: 10339414
DOI: 10.1006/jmbi.1999.2742

Experimental method

SOLUTION NMR